Structure of PDB 3hf2 Chain A

Receptor sequence
>3hf2A (length=428) Species: 1404 (Priestia megaterium) [Search protein sequence]
MPQPKTFGELKNLPLLNTDKPVQALMKIADELGEIFKFEAPGRVTRYLSS
QRLIKEACDESRFDKNLSQALKFVRDFAGDGLFTSWTHEKNWKKAHNILL
PSFSQQAMKGYHAMMVDIAVQLVQKWERLNADEHIEVPEDMTRLTLDTIG
LCGFNYRFNSFYRDQPHSMVRALDEAMENKRQFQEDIKVMNDLVDKIIAD
RQSDDLLTHMLNGKDPETGEPLDDENIRYQIITFLIAGHETTSGLLSFAL
YFLVKNPHVLQKAAEEAARVLVDPVPSYKQVKQLKYVGMVLNEALRLWPT
APAFSLYAKEDTVLGGEYPLEKGDELMVLIPQLHRDKTIWGDDVEEFRPE
RFENPSAIPQHAFKPFGNGQRACPGQQFALHEATLVLGMMLKHFDFEDHT
NYELDIKETLTLKPEGFVVKAKSKKIPL
3D structure
PDB3hf2 A Highly Active Single-Mutation Variant of P450(BM3) (CYP102A1)
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) T268 F393 C400
Catalytic site (residue number reindexed from 1) T241 F366 C373
Enzyme Commision number 1.14.14.1: unspecific monooxygenase.
1.6.2.4: NADPH--hemoprotein reductase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A K69 L86 F87 W96 A264 G265 T268 T269 F331 P392 F393 G394 R398 C400 P401 G402 A406 K65 L82 F83 W92 A237 G238 T241 T242 F304 P365 F366 G367 R371 C373 P374 G375 A379
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0020037 heme binding

View graph for
Molecular Function
External links
PDB RCSB:3hf2, PDBe:3hf2, PDBj:3hf2
PDBsum3hf2
PubMed19492389
UniProtP14779|CPXB_PRIM2 Bifunctional cytochrome P450/NADPH--P450 reductase (Gene Name=cyp102A1)

[Back to BioLiP]